INVESTIGADORES
MARTIN Osvaldo Antonio
congresos y reuniones científicas
Título:
Modelling of Three Dimensional Structure of Trypanosoma cruzi Ribosomal P Proteins and Their Interactions
Autor/es:
MARTIN, OSVALDO; AGUILAR, CARLOS; VILLEGAS, MYRIAM; VILA, JORGE
Lugar:
Montevideo
Reunión:
Congreso; 6th International Conference of Biological Physics, 5th Southern Cone Biophysics Congress and 34th Annual Meeting of the Argentinean Biophysical Society; 2007
Institución organizadora:
International Union for Pure and Applied Biophysics, Sociedad Argentina de Biofísica, Sociedad Uruguaya de Biociencias
Resumen:
Ribosomal P proteins are a complex of proteins which form a long and protruding region, called the stalk in the large subunit of the ribosome. In eukaryotes the P family encompasses protein P0 (34 kD), P1 and P2 (~10kD). The number of proteins in the P1 and P2 families varies among species. In mammals the complex is formed by P0 and two copies of P1 and P2 but Saccharomyces cerevisiae and Trypanosoma cruzi, the parasite that produces Chagas disease, have five members: P0, P1(alpha), P1(beta) P2(alpha) and P2(beta). ). All of them have a conserved acidic motif in the C-terminal end and show high sequence identity with P0 C-terminal (last one hundred amino acids). Experimental evidence suggest that T. cruzi P1-P2 proteins and the CTD of P0 belong to a new class of proteins called natively unfoldedor Intrinsically Unstructured Proteins (IUPs) The structure of T. cruzi P0 and the stalk complex P0- P1(alpha)P1(beta)-P2(alpha) -P2(beta) has not been solved up to date. The aim of this work is to correlate previous structural information and calculate models for P0, P1(alpha), P1(beta), P2(alpha) and P2(beta). This is the first step toward the analysis of possible ways of interaction of Ribosomal P proteins among themselves.